ID   C5EYJ3_9HELI            Unreviewed;       184 AA.
AC   C5EYJ3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893, ECO:0000256|HAMAP-Rule:MF_00004};
DE            Short=APRT {ECO:0000256|HAMAP-Rule:MF_00004};
DE            EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893, ECO:0000256|HAMAP-Rule:MF_00004};
GN   Name=apt {ECO:0000256|HAMAP-Rule:MF_00004,
GN   ECO:0000313|EMBL:EEQ63341.1};
GN   ORFNames=HPMG_00798 {ECO:0000313|EMBL:EEQ63341.1};
OS   Helicobacter pullorum MIT 98-5489.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537972 {ECO:0000313|EMBL:EEQ63341.1};
RN   [1] {ECO:0000313|EMBL:EEQ63341.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MIT 98-5489 {ECO:0000313|EMBL:EEQ63341.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T.,
RA   Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T.,
RA   Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Helicobacter pullorum strain MIT 98-5489.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC       AMP, that is energically less costly than de novo synthesis.
CC       {ECO:0000256|ARBA:ARBA00003968, ECO:0000256|HAMAP-Rule:MF_00004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000868, ECO:0000256|HAMAP-
CC         Rule:MF_00004};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenine: step 1/1. {ECO:0000256|ARBA:ARBA00004659,
CC       ECO:0000256|HAMAP-Rule:MF_00004}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00004}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00008391, ECO:0000256|HAMAP-
CC       Rule:MF_00004}.
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DR   EMBL; DS990442; EEQ63341.1; -; Genomic_DNA.
DR   RefSeq; WP_005021649.1; NZ_DS990442.1.
DR   AlphaFoldDB; C5EYJ3; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_063339_3_0_7; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000003953; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-UniRule.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR   InterPro; IPR005764; Ade_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   NCBIfam; TIGR01090; apt; 1.
DR   PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR32315:SF3; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00004};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00004};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW   Rule:MF_00004};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00004}.
FT   DOMAIN          32..183
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   184 AA;  20717 MW;  D8293CB1B322C061 CRC64;
     MELTQQEKNM LLDSIREIKD FPQPGIVFRD ITTLLNNKEA YSFLMDSLSR RYRDYHLDYV
     AGIESRGFIF GAALAYSLGI GFVPIRKKGK LPYTTISEKY SLEYGFSEIE IHIDAFKNHS
     LEHAPKVLLI DDLIATGGTA YAAANLIKKA GAECVESCFI INLQELKGAE ELKKITPVYS
     VLEI
//